Cold denaturation of ubiquitin
โ Scribed by Beatriz Ibarra-Molero; George I. Makhatadze; Jose M. Sanchez-Ruiz
- Book ID
- 114149840
- Publisher
- Elsevier Science
- Year
- 1999
- Tongue
- English
- Weight
- 245 KB
- Volume
- 1429
- Category
- Article
- ISSN
- 0167-4838
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๐ SIMILAR VOLUMES
Cold-induced conformational transition of ubiquitin was studied at pH 4.5 under a constant pressure of 2 kbar using variable pressure one-dimensional 1H and two-dimensional 15N/1H NMR spectroscopy as well as IR spectroscopy. Although a tendency for preferential stabilization of a peculiar locally di
We have investigated the thermal unfolding of bovine โฃ-lactalbumin by means of circular dichroism spectroscopy in the far-and nearultraviolet regions, and shown that the native โฃ-lactalbumin undergoes heat and cold denaturation. The guanidine hydrochloride-induced unfolding of โฃ-lactalbumin was also